The Pseudomonas aeruginosa PAO1 metallo flavoprotein d-2-hydroxyglutarate dehydrogenase requires Zn²⁺ for substrate orientation and activation.

ABSTRACT: Pseudomonas aeruginosa PAO1 d-2-hydroxyglutarate (D2HG) dehydrogenase (PaD2HGDH) oxidizes D2HG to 2-ketoglutarate during the vital l-serine biosynthesis and is a potential therapeutic target against P. aeruginosa. PaD2HGDH, which oxidizes d-malate as an alternative substrate, has been demonstrated to be a metallo flavoprotein that requires Zn²⁺ for activity. However, the role of Zn²⁺ in the enzyme has not been elucidated, making it difficult to rationalize why nature employs both a redox center and a metal ion for catalysis in PaD2HGDH and other metallo flavoenzymes. In this study, recombinant His-tagged PaD2HGDH was purified to high levels in the presence of Zn²⁺ or Co²⁺ to investigate the metal's role in catalysis. We found that the flavin redu

SUBMITTER: Quaye JA 

PROVIDER: S-EPMC10034468 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature